The basic helix-loop-helix transcription factor, HES3, acts downstream of the PAX3-FOXO1 fusion oncogene to impair muscle differentiation and promote tumorigenesis in rhabdomyosarcoma, a childhood muscle cancer.
The structural basis for Her2's role as a dedicated heterodimerization partner for other EGFR family receptors is elucidated with long-timescale atomistic simulations.
The clinically approved HER2 inhibitor lapatinib causes HER2 and HER3 kinase domains to dimerise in a non-canonical, symmetric orientation, providing a platform for oligomerisation and predisposing to receptor-driven cell proliferation.
Conservative mutations within a secondary active transport protein influenced the conformational equilibrium probed using NMR spectroscopy which correlated to the functional output in vivo.
Single-molecule immunoprecipitation method reveals that the high catalytic rate and multi-tasking capability make a concerted contribution to the strong signaling potency of the HER2-HER3 heterodimers.